We present the three-dimensional structure of the N-terminal FK506-binding
protein (FKBP)-like domain of the immunophilin FKBP42 from Arabidopsis thaliana.
The data provide the structural background for the explanation of key functional
properties reported previously.
Figure 1.
Fig. 1. Superposition of the crystal structures of
AtFKBP42^1-180 (blue), HsFKBP12 (grey) and AtFKBP13 (orange).
Secondary structure elements of the canonical FKBP fold are
numbered consecutively; β0 is an additional β-strand present
in AtFKBP42^1-180. The FK506 molecule bound to HsFKBP12 is shown
as stick model.
Figure 3.
Fig. 3. Comparison of the molecular surfaces of HsFKBP12
(A) and AtFKBP42^1-180 (B). The FK506 ligand (dark grey) is
positioned as in the complex with HsFKBP12. Orientation of the
molecules is the same as in Fig. 2.
The above figures are
reprinted
by permission from the Federation of European Biochemical Societies:
FEBS Lett
(2006,
580,
251-255)
copyright 2006.
